The Crystal Structures of Man(α1–3)Man(α1-O)Me and Man(α1–6)Man(α1-O)Me in Complex with Concanavalin A

Structural Basis of Oligomannose Recognition by the Pterocarpus angolensis Seed Lectin

“…All three disaccharides make at least one additional hydrogen bond with amino acid residues in the þ 1 site. This situation is similar to what has been observed for ConA, 31 where Man(a1-6)Man binds with the same affinity as MeaMan, despite an additional hydrogen bond from the protein to the reducing mannose. Figure 7 compares the binding modes of Man(a1-3)Man and Man(a1-6)Man with those observed previously in their complexes with ConA.…”

“…Figure 7 compares the binding modes of Man(a1-3)Man and Man(a1-6)Man with those observed previously in their complexes with ConA. 31 Man(a1-3)Man binds in an identical conformation and orientation to ConA and PAL, although the residues that make up subsite þ 1 differ in both proteins (Figure 7(a)). Man(a1-6)Man recognition on the other hand is different in both proteins, and the disaccharides adopt different low-energy conformations (Figure 7(b)).…”

Carbohydrate-mimetic peptides: structural aspects of mimicry and therapeutic implications

“…5CNA a-Man-(1-OMe) 2.00 [66] 1I3H a-Man-(1!2)-a-Man 1.20 [67] 1QDO a-Man-(1!3)-a-Man-(1-OMe) 2.80 [68] 1QDC a-Man-(1!6)-a-Man-(1-OMe) 2.00 [68] 1CVN 1GIC a-Glc-(1-OMe) 2.00 [63] 1JYI DVFYPYPYASGS 2.75 [71] 1JOJ Ace-MYWYPY-NH 2 3.00 2G12 ( Figure 3E). Therefore, the peptide is not a structural mimic of Man 9 GlcNAc 2 .…”

“…Since its isolation from the seeds of the jack bean (Canavalia ensiformis) almost 100 years ago, it has become one of the most widely studied lectins [65]. A large number of crystal structures of ConA in complex with various carbohydrates [63,[66][67][68][69][70] and peptides [47,[71][72][73] have been published (Table 3), allowing for thorough comparison of carbohydrate and peptide recognition by this lectin.…”

Evaluation of two different Concanavalin A affinity adsorbents for the adsorption of glucose oxidase

“…One of them is suitable for the binding of a transition metal such as manganese, whereas the other one binds calcium. The crystal structures of Con A with a series of carbohydrates have been extensively studied; the results show that the affinity binding is mainly based on hydrogen bonds and Van der Waals interactions [12,13]. Immobilized Con A is widely employed for the affinity purification and separation of glycoenzymes [14][15][16].…”